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Database: UniProt
Entry: A0A1I2VWD6_9BACL
LinkDB: A0A1I2VWD6_9BACL
Original site: A0A1I2VWD6_9BACL 
ID   A0A1I2VWD6_9BACL        Unreviewed;       586 AA.
AC   A0A1I2VWD6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   ORFNames=SAMN02982927_03220 {ECO:0000313|EMBL:SFG91641.1};
OS   Sporolactobacillus nakayamae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Sporolactobacillaceae;
OC   Sporolactobacillus.
OX   NCBI_TaxID=269670 {ECO:0000313|EMBL:SFG91641.1, ECO:0000313|Proteomes:UP000198752};
RN   [1] {ECO:0000313|EMBL:SFG91641.1, ECO:0000313|Proteomes:UP000198752}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700379 {ECO:0000313|EMBL:SFG91641.1,
RC   ECO:0000313|Proteomes:UP000198752};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + sn-glycerol 3-phosphate = a quinol +
CC         dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:132124; EC=1.1.5.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00000153,
CC         ECO:0000256|RuleBase:RU361217};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU361217};
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC       pathway; glycerone phosphate from sn-glycerol 3-phosphate (aerobic
CC       route): step 1/1. {ECO:0000256|ARBA:ARBA00004977}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330,
CC       ECO:0000256|RuleBase:RU361217}.
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DR   EMBL; FOOY01000029; SFG91641.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2VWD6; -.
DR   STRING; 269670.SAMN02982927_03220; -.
DR   UniPathway; UPA00618; UER00674.
DR   Proteomes; UP000198752; Unassembled WGS sequence.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.8.870; Alpha-glycerophosphate oxidase, cap domain; 1.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR031656; DAO_C.
DR   InterPro; IPR038299; DAO_C_sf.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000447; G3P_DH_FAD-dep.
DR   PANTHER; PTHR11985:SF37; AEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16901; DAO_C; 1.
DR   PRINTS; PR01001; FADG3PDH.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00977; FAD_G3PDH_1; 1.
DR   PROSITE; PS00978; FAD_G3PDH_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU361217};
KW   Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361217}.
FT   DOMAIN          43..400
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          428..556
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   586 AA;  65755 MW;  839505DD03330563 CRC64;
     MVFFYMDEMP SSAYKFENGG MNRMLSTFNR NEYLEKMAGN PLDLFIIGGG ITGAGIALDA
     TVRGLKVGLV DMQDFAGGTS SKSTKLVHGG LRYLKQFEVK IVAEVGKERA IVYENAPHVT
     TPEKMMLPIY KGGTFGRFST SLGLKVYDFL AGVKKEERRV MFSRKETLAK EPLLKKEGLK
     GSGYYVEYRT DDARLTIEVI KEASDRGALA VNYAKVEDLI YNQKKKLIGV RVVDRLTKKE
     YSIFAKKIVN AAGPWVDTIR ERDHSKKGKH LHLTKGVHIV IDGKRFPMKQ SVYFDTTNGD
     KRMLFVIPRE GKVYAGTTDT TYSRWPIDPK PTAEDRDYIL DAINGMFPSV HLTSDDVESS
     WAGVRPLIQE EGKSPSEISR KDEIFISRSG LISIAGGKLT GYRKMAERVV DEVAAQLHRE
     GGKTYPACRT AHIELSGGHF GGSTHYATYV QEQKQIGIGL GLTEKEAEEL AKKYGTNIGE
     LFGYIQMNQE EAKKYQLPPA LLAAVHYALT HEMILSPVDY FTRRSGMTLF SIQSARKWAQ
     PVTDYMAEQL QWSDQQTKEY ARELEAAFNE ASPYETTSDV SETKRV
//
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